| Project/Area Number |
22570166
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biophysics
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| Research Institution | The Institute of Physical and Chemical Research |
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Principal Investigator |
YUTANI Katsuhide 独立行政法人理化学研究所, タンパク質結晶構造解析研究グループ, 上級研究員 (90089889)
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| Co-Investigator(Renkei-kenkyūsha) |
MATSUURA Yoshinori 独立行政法人理化学研究所, タンパク質結晶構造解析研究グループ, リサーチアソシエイト (50513462)
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| Project Period (FY) |
2010 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2012: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2011: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2010: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | 蛋白質変性の熱力学 / 蛋白質の安定性 / 蛋白質熱変性の可逆性 / 示差走査熱量計 / 超好熱菌由来蛋白質 / 疎水性相互作用 / イオン相互作用 / CutA1 / DSC / 熱変性の可逆性 / 蛋白質の立体構造 / 蛋白質の熱変性 / 蛋白質の構造 / CutAl |
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| Research Abstract |
The heat-denaturation of proteins is usually irreversible at higher temperatures than around 70℃, because of aggregation after heat denaturation. Therefore, their thermodynamic characteristics are less well understood at the temperatures more than 70℃. In this study, we found that SH-free CutA1 mutant from E. coli and its hydrophobic mutants show very good reversibility of heat denaturation at pH 9. The denaturation temperatures of the hydrophobic mutants were 90-115℃. Then, we succeeded to experimentally obtain the thermodynamic parameters of protein denaturation over 100℃ by DSC.
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